Which of the following statements regarding enzyme catalysis is false?All options are false.Once formed, the transition state slowly proceeds to forming the product at a rate determinedby cofactor bindingThe free energy of binding of the enzyme to the transition state is more favorable than the freeenergy of binding of the enzyme to the substrateThe substrate and active site of the enzyme are solvated to promote enzyme-substrateinteractionOnce formed, the product dissociates from the enzyme after ATP hydrolysis in order toregenerate the active site

Biochemical reaction tend to be slow, unlikely or unfavorable in the chemical environment is the…

Answered: Which of the following statements…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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on When testing the effect of substrate concentration on the reaction rate, there comes a point at which increasing the substrate concentration has no effect on the reaction rate. That is, the reaction rate remains the same and no longer increases. Which of the statements below would explain this? Select one: O A. The enzyme is denatured OB. The substrate is denatured OC. All available enzymes are saturated or full with substrates. OD. The enzyme concentration is too high
A catalase is an antioxidant enzyme that requires ferric ion for catalysis. Under conditions of iron deficiency, when the catalase lacks ferric ion, it would be referred to as: O prosthetic group O holoenzyme ароenzyme coenzyme
The induced-fit theory aims to explain how the interactions between an enzyme and a sub- strate facilitate the catalysis of chemical reactions. Which of the following properties of enzyme-substrate interaction best explains enzymatic catalysis according to the induced-fit model? A B с D Environmental conditions can alter the affinity between a substrate and an enzyme by changing the conformation of the enzyme. Conformation changes in both the enzyme and the substrate due to their chemical in- teractions lower the activation energy of the catalyzed reactions. The interactions between an enzyme and a substrate depend on both structural and chemical compatibility and are therefore highly specific. Enzymes remain chemically unaltered between cycles of enzymatic catalysis while sub- strates are transformed into products.
Which of the following is the typical shape of a plot showing the rate of an enzyme-catalyzed reaction as a function of the enzyme concentration with excess substrate?
Indicate whether each of the following statements about an enzyme active site is true or false. It is the location where substrate molecules are produced. It always has a fixed, rigid geometry. It always has a geometrical shape exactly complementary to that of substrate. It always accommodates several structurally related substrates. It is the location where substrate molecules are converted to product molecules. It always has a shape that has a degree of flexibility to it. It always accommodates only one specific substrate.
What enzyme kinetic parameters are apparantly impacted by uncompetitive inhibitors? Vmax Km Both Km and Vmax Neither Km nor Vmax
When reviewing a Michaelis-Menten Saturation Curve, at first the rate of the reaction is relatively constant, but the rate decreases as the substrate is used up and eventually reaches a plateau. Afte reaching this plateau, what would speed up the reaction again? Adding more substrate Adding heat Adding more enzyme Adding cofactors
Please handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.
The 2 eynzymes are affected by a substrate. Choose all correct answers.
kcat is: a measure of the catalytic efficiency of the enzyme the rate constant for the reaction ES → E + P the rate constant for the reaction ES → E + S the [S] that half saturates the enzyme ½ Vmax
Catalysis through proximity and orientation effects involves: (select all that applies) Group of answer choices binding of acidic and/or basic groups in the binding site facilitating chemical reactions by binding substrates close to specific groups binding of substrate in specific, restrictive orientations depending on metal ions for catalysis
None

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